Effects of inorganic selenium compounds on oxidative DNA damage

Ramoutar, Ria R.; Brumaghim, Julia L.

doi:10.1016/j.jinorgbio.2007.03.016

Cited by 60 publications

(64 citation statements)

References 46 publications

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“…SeMet participates in an intramolecular transsulfuration reaction, forming selenocystein, which, in turn, increases the activity of internal antioxidant enzymes GPX and thioredoxin reductase (1). In addition, SeMet is able to directly interact with some oxidant molecules or oxidant-generating ions (3,43). Ginsenosides act as antioxidants by increasing internal antioxidant enzymes and acting as free-radical scavengers (11,34,48,52).…”

Section: H198 Resistin Causes Endothelial Dysfunctionmentioning

confidence: 99%

Resistin decreases expression of endothelial nitric oxide synthase through oxidative stress in human coronary artery endothelial cells

Chen

Jiang

Lü

et al. 2010

American Journal of Physiology-Heart and Circulatory Physiology

174

114

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Resistin decreases expression of endothelial nitric oxide synthase through oxidative stress in human coronary artery endothelial cells. Am J Physiol Heart Circ Physiol 299: H193-H201, 2010. First published April 30, 2010 doi:10.1152/ajpheart.00431.2009.-Resistin is a newly discovered adipocyte-derived cytokine that may play an important role in insulin resistance, diabetes, adipogenesis, inflammation, and cardiovascular disease. However, it is largely unknown whether resistin impairs endothelial functions by affecting the endothelial nitric oxide synthase (eNOS) system. In this study, we determined the effect of human recombinant resistin protein on eNOS expression and regulation in human coronary artery endothelial cells (HCAECs). When cells were treated with clinically relevant concentrations of resistin (40 or 80 ng/ml) for 24 h, the levels of eNOS mRNA, protein, and activity and eNOS mRNA stability were significantly reduced. Cellular nitric oxide levels were also decreased. In addition, the cellular levels of reactive oxygen species (ROS), including superoxide anion, were significantly increased in resistin-treated HCAECs. Mitochondrial membrane potential and the activities of catalase and superoxide dismutase were reduced. Three antioxidants, seleno-L-methionine, ginsenoside Rb1, and MnTBAP (superoxide dismutase mimetic), effectively blocked resistin-induced eNOS downregulation. Meanwhile, resistin activated the mitogen-activated protein kinases p38 and c-Jun NH2-terminal kinase (JNK), and the specific p38 inhibitor SB-239063 effectively blocked resistin-induced ROS production and eNOS downregulation. Furthermore, immunoreactivity of resistin was increased in atherosclerotic regions of human aorta and carotid arteries. Thus resistin directly induces eNOS downregulation through overproduction of ROS and activation of p38 and JNK in HCAECs. Resistin-induced mitochondrial dysfunction and imbalance in cellular redox enzymes may be the underlying mechanisms of oxidative stress.

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Section: H198 Resistin Causes Endothelial Dysfunctionmentioning

confidence: 99%

Resistin decreases expression of endothelial nitric oxide synthase through oxidative stress in human coronary artery endothelial cells

Chen

Jiang

Lü

et al. 2010

American Journal of Physiology-Heart and Circulatory Physiology

174

114

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“…As reviewed by Battin and Brumaghim (2009), numerous Se compounds have been suggested to exert antioxidant activity through a coordination of metal ions. For example, sodium selenite (Na 2 SeO 3 ) and selenium dioxide (SeO 2 ) were shown to inhibit oxidative DNA damage caused by iron (Fe 2+ ) in the presence of H 2 O 2 , in a cell free system, which contained plasmid DNA, Fe 2+ and H 2 O 2 (Ramoutar and Brumaghim 2007). Since no selenium-related inhibitory effect on DNA damage in this experiment was observed when iron was completely coordinated to EDTA [Fe (EDTA)] 2− , it was concluded that iron coordination by Na 2 SeO 3 and SeO 2 is required for inhibition of DNA damage (Ramoutar and Brumaghim 2007).…”

mentioning

confidence: 99%

“…For example, sodium selenite (Na 2 SeO 3 ) and selenium dioxide (SeO 2 ) were shown to inhibit oxidative DNA damage caused by iron (Fe 2+ ) in the presence of H 2 O 2 , in a cell free system, which contained plasmid DNA, Fe 2+ and H 2 O 2 (Ramoutar and Brumaghim 2007). Since no selenium-related inhibitory effect on DNA damage in this experiment was observed when iron was completely coordinated to EDTA [Fe (EDTA)] 2− , it was concluded that iron coordination by Na 2 SeO 3 and SeO 2 is required for inhibition of DNA damage (Ramoutar and Brumaghim 2007). Similarly, another in vitro study reported inhibition of iron-and copper-mediated oxidative DNA damage by organoselenium compounds, selenocystine, selenomethionine, and methylselenocysteine due to the metal-binding mechanism (Battin et al 2011).…”

mentioning

confidence: 99%

Selenium interactions and toxicity: a review

2011

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Selenium is an essential trace element for mammals. Through selenoproteins, this mineral participates in various biological processes such as antioxidant defence, thyroid hormone production, and immune responses. Some reports indicate that a human organism deficient in selenium may be prone to certain diseases. Adverse health effects following selenium overexposure, although very rare, have been found in animals and people. Contrary to selenium, arsenic and cadmium are regarded as toxic elements. Both are environmental and industrial pollutants, and exposure to excessive amounts of arsenic or cadmium can pose a threat to many people's health, especially those living in polluted regions. Two other elements, vanadium and chromium(III) in trace amounts are believed to play essential physiological functions in mammals. This review summarizes recent studies on selenium interactions with arsenic and cadmium and selenium interactions with vanadium and chromium in mammals. Human studies have demonstrated that selenium may reduce arsenic accumulation in the organism and protect against arsenic-related skin lesions. Selenium was found to antagonise the prooxidant and genotoxic effects of arsenic in rodents and cell cultures. Also, studies on selenium effects against oxidative stress induced by cadmium in various animal tissues produced promising results. Reports suggest that selenium protection against toxicity of arsenic and cadmium is mediated via sequestration of these elements into biologically inert conjugates. Selenium-dependent antioxidant enzymes probably play a secondary role in arsenic and cadmium detoxification. So far, few studies have evaluated selenium effects on chromium(III) and vanadium actions in mammals. Still, they show that selenium may interact with these minerals. Taken together, the recent findings regarding selenium interaction with other elements extend our understanding of selenium biological functions and highlight selenium as a potential countermeasure against toxicity induced by arsenic and cadmium.

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“…Methyl-selenocysteine exhibited the ability to minimize oxidative DNA damage by coordinating both Cu(I) and Fe(II), and whereas selenocystamine exhibited antioxidant activity for reactions involving both Cu(I) and Fe(II), there was evidence that it formed a coordination complex only with Fe(II) (56). The inorganic Se compounds Se dioxide (SeO 2 ) and sodium selenite [Na 2 SeO 3 , which dissociates in aqueous solution to produce the selenite ion (SeO 3 2-)], also appear to function as antioxidants in reactions involving Fe(II), Cu(II), and Cr(III) by coordinating these metal ions (57,58). All of these compounds exhibit different levels of protection, and the extent of antioxidant behavior also depends on the identity of the metal ion.…”

Section: Selenium Compoundsmentioning

confidence: 99%

DNA-bound metal ions: recent developments

Morris

2014

Biomolecular Concepts

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Abstract:The affinity of metal ions for DNA is logical considering that the structure of DNA includes a phosphate backbone with a net-negative charge, a deoxyribose sugar with O atoms, and purine and pyrimidine bases that contain O and N atoms. DNA-metal ion interactions encompass a large area of research that ranges from the most fundamental characterization of DNA-metal ion binding to the role of DNA-bound metal ions in disease and human health. Alternative DNA base pairing mediated by metal binding is also being investigated and manipulated for applications in logic gates, molecular machines, and nanotechnology. This review highlights recent work aimed at understanding interactions of redox-active metal ions with DNA that provides a better understanding of the mechanisms by which various types of oxidative DNA damage (strand breakage and base modifications) occur. Antioxidants that mitigate oxidative DNA damage by coordinating metal ions that produce reactive oxygen species are addressed, as well as recent work on the effect of DNAmetal ion interactions and the efficacy of quinolone-based antibacterial drugs. Recent advances in metal-mediated base pairing that triggers conformational changes in DNA structure for use as selective metal ion sensors and novel nanotechnology applications are also included.

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Effects of inorganic selenium compounds on oxidative DNA damage

Cited by 60 publications

References 46 publications

Resistin decreases expression of endothelial nitric oxide synthase through oxidative stress in human coronary artery endothelial cells

Resistin decreases expression of endothelial nitric oxide synthase through oxidative stress in human coronary artery endothelial cells

Selenium interactions and toxicity: a review

DNA-bound metal ions: recent developments

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